6Z2T
Three-dimensional structure of an influenza hemagglutinin LAH protein in its post-fusion conformation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-3 |
Synchrotron site | MAX II |
Beamline | I911-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-04-01 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.91841 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 36.780, 36.780, 166.570 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 41.680 - 1.340 |
R-factor | 0.2165 |
Rwork | 0.215 |
R-free | 0.23840 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6gol |
RMSD bond length | 0.012 |
RMSD bond angle | 1.756 |
Data scaling software | SCALA |
Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 55.520 | 1.420 |
High resolution limit [Å] | 1.340 | 1.340 |
Rmerge | 0.050 | 0.583 |
Number of reflections | 15916 | 2234 |
<I/σ(I)> | 13.3 | 2.5 |
Completeness [%] | 99.5 | 98.4 |
Redundancy | 7.1 | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.7 | 294 | 0.15 M H6NO4P and 40% MPD; pH 6.7; protein 10 mg/mL |